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PDBsum entry 1j1h
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RNA binding protein
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PDB id
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1j1h
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Contents |
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* Residue conservation analysis
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PDB id:
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RNA binding protein
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Title:
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Solution structure of a tmrna-binding protein, smpb, from thermus thermophilus
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Structure:
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Small protein b. Chain: a. Engineered: yes
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Source:
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Thermus thermophilus. Organism_taxid: 274. Expressed in: escherichia coli. Expression_system_taxid: 562.
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NMR struc:
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11 models
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Authors:
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T.Someya,N.Nameki,H.Hosoi,S.Suzuki,H.Hatanaka,M.Fujii,T.Terada, M.Shirouzu,Y.Inoue,T.Shibata,S.Kuramitsu,S.Yokoyama,G.Kawai,Riken Structural Genomics/proteomics Initiative (Rsgi)
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Key ref:
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T.Someya
et al.
(2003).
Solution structure of a tmRNA-binding protein, SmpB, from Thermus thermophilus.
FEBS Lett,
535,
94.
PubMed id:
DOI:
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Date:
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04-Dec-02
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Release date:
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11-Feb-03
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PROCHECK
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Headers
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References
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Q8RR57
(SSRP_THET8) -
SsrA-binding protein from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
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Seq: Struc:
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144 a.a.
123 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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FEBS Lett
535:94
(2003)
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PubMed id:
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Solution structure of a tmRNA-binding protein, SmpB, from Thermus thermophilus.
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T.Someya,
N.Nameki,
H.Hosoi,
S.Suzuki,
H.Hatanaka,
M.Fujii,
T.Terada,
M.Shirouzu,
Y.Inoue,
T.Shibata,
S.Kuramitsu,
S.Yokoyama,
G.Kawai.
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ABSTRACT
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Small protein B (SmpB) is required for trans-translation, binding specifically
to tmRNA. We show here the solution structure of SmpB from an extremely
thermophilic bacterium, Thermus thermophilus HB8, determined by heteronuclear
nuclear magnetic resonance methods. The core of the protein consists of an
antiparallel beta-barrel twisted up from eight beta-strands, each end of which
is capped with the second or third helix, and the first helix is located beside
the barrel. Its C-terminal sequence (20 residues), which is rich in basic
residues, shows a poorly structured form, as often seen in isolated ribosomal
proteins. The results are discussed in relation to the oligonucleotide binding
fold.
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Selected figure(s)
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Figure 1.
Fig. 1. ^1H–^15N HSQC spectrum of SmpB from T.
thermophilus. Resonance assignments from residue 4 to 123 are
labeled according to the residue position in the protein
sequence, and the side chain NH[2] signals are connected and
labeled by residue type and number. Unassigned signals are
indicated by solid circles.
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Figure 2.
Fig. 2. Solution structures of SmpB from T. thermophilus.
a: Stereo view of the final ensemble 10 structures superimposed
on ordered regions (residues 8–62 and 79–122). Residues
124–144 are not depicted. b: Ribbon diagrams of the average
structure of SmpB. The two views differ by a 90° rotation. The
diagrams were created using the MOLMOL program [22].
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The above figures are
reprinted
by permission from the Federation of European Biochemical Societies:
FEBS Lett
(2003,
535,
94-0)
copyright 2003.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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Y.Chadani,
K.Ono,
K.Kutsukake,
and
T.Abo
(2011).
Escherichia coli YaeJ protein mediates a novel ribosome-rescue pathway distinct from SsrA- and ArfA-mediated pathways.
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Mol Microbiol,
80,
772-785.
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D.Kurita,
A.Muto,
and
H.Himeno
(2010).
Role of the C-terminal tail of SmpB in the early stage of trans-translation.
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RNA,
16,
980-990.
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F.Weis,
P.Bron,
E.Giudice,
J.P.Rolland,
D.Thomas,
B.Felden,
and
R.Gillet
(2010).
tmRNA-SmpB: a journey to the centre of the bacterial ribosome.
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EMBO J,
29,
3810-3818.
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PDB codes:
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F.Weis,
P.Bron,
J.P.Rolland,
D.Thomas,
B.Felden,
and
R.Gillet
(2010).
Accommodation of tmRNA-SmpB into stalled ribosomes: a cryo-EM study.
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RNA,
16,
299-306.
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J.Richards,
T.Sundermeier,
A.Svetlanov,
and
A.W.Karzai
(2008).
Quality control of bacterial mRNA decoding and decay.
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Biochim Biophys Acta,
1779,
574-582.
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L.Metzinger,
M.Hallier,
and
B.Felden
(2008).
The highest affinity binding site of small protein B on transfer messenger RNA is outside the tRNA domain.
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RNA,
14,
1761-1772.
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D.Kurita,
R.Sasaki,
A.Muto,
and
H.Himeno
(2007).
Interaction of SmpB with ribosome from directed hydroxyl radical probing.
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Nucleic Acids Res,
35,
7248-7255.
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K.Takada,
C.Takemoto,
M.Kawazoe,
T.Konno,
K.Hanawa-Suetsugu,
S.Lee,
M.Shirouzu,
S.Yokoyama,
A.Muto,
and
H.Himeno
(2007).
In vitro trans-translation of Thermus thermophilus: ribosomal protein S1 is not required for the early stage of trans-translation.
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RNA,
13,
503-510.
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S.D.Moore,
and
R.T.Sauer
(2007).
The tmRNA system for translational surveillance and ribosome rescue.
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Annu Rev Biochem,
76,
101-124.
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T.Konno,
D.Kurita,
K.Takada,
A.Muto,
and
H.Himeno
(2007).
A functional interaction of SmpB with tmRNA for determination of the resuming point of trans-translation.
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RNA,
13,
1723-1731.
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Y.Bessho,
R.Shibata,
S.Sekine,
K.Murayama,
K.Higashijima,
C.Hori-Takemoto,
M.Shirouzu,
S.Kuramitsu,
and
S.Yokoyama
(2007).
Structural basis for functional mimicry of long-variable-arm tRNA by transfer-messenger RNA.
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Proc Natl Acad Sci U S A,
104,
8293-8298.
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PDB codes:
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D.P.Dulebohn,
H.J.Cho,
and
A.W.Karzai
(2006).
Role of conserved surface amino acids in binding of SmpB protein to SsrA RNA.
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J Biol Chem,
281,
28536-28545.
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M.Hallier,
J.Desreac,
and
B.Felden
(2006).
Small protein B interacts with the large and the small subunits of a stalled ribosome during trans-translation.
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Nucleic Acids Res,
34,
1935-1943.
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L.Metzinger,
M.Hallier,
and
B.Felden
(2005).
Independent binding sites of small protein B onto transfer-messenger RNA during trans-translation.
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Nucleic Acids Res,
33,
2384-2394.
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N.Ivanova,
M.Y.Pavlov,
E.Bouakaz,
M.Ehrenberg,
and
L.H.Schiavone
(2005).
Mapping the interaction of SmpB with ribosomes by footprinting of ribosomal RNA.
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Nucleic Acids Res,
33,
3529-3539.
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T.R.Sundermeier,
D.P.Dulebohn,
H.J.Cho,
and
A.W.Karzai
(2005).
A previously uncharacterized role for small protein B (SmpB) in transfer messenger RNA-mediated trans-translation.
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Proc Natl Acad Sci U S A,
102,
2316-2321.
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Y.Jacob,
S.M.Sharkady,
K.Bhardwaj,
A.Sanda,
and
K.P.Williams
(2005).
Function of the SmpB tail in transfer-messenger RNA translation revealed by a nucleus-encoded form.
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J Biol Chem,
280,
5503-5509.
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P.W.Haebel,
S.Gutmann,
and
N.Ban
(2004).
Dial tm for rescue: tmRNA engages ribosomes stalled on defective mRNAs.
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Curr Opin Struct Biol,
14,
58-65.
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T.Okada,
I.K.Wower,
J.Wower,
C.W.Zwieb,
and
M.Kimura
(2004).
Contribution of the second OB fold of ribosomal protein S1 from Escherichia coli to the recognition of TmRNA.
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Biosci Biotechnol Biochem,
68,
2319-2325.
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S.Gutmann,
P.W.Haebel,
L.Metzinger,
M.Sutter,
B.Felden,
and
N.Ban
(2003).
Crystal structure of the transfer-RNA domain of transfer-messenger RNA in complex with SmpB.
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Nature,
424,
699-703.
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PDB code:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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